4R4Y

Structural basis of a point mutation that causes the genetic disease Aspartylglucosaminuria

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003948	molecular_function	N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity
A	0004067	molecular_function	asparaginase activity
A	0005737	cellular_component	cytoplasm
A	0006508	biological_process	proteolysis
A	0006517	biological_process	protein deglycosylation
A	0008233	molecular_function	peptidase activity
A	0008798	molecular_function	beta-aspartyl-peptidase activity
A	0016787	molecular_function	hydrolase activity
A	0042597	cellular_component	periplasmic space
B	0003948	molecular_function	N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity
B	0004067	molecular_function	asparaginase activity
B	0005737	cellular_component	cytoplasm
B	0006508	biological_process	proteolysis
B	0006517	biological_process	protein deglycosylation
B	0008233	molecular_function	peptidase activity
B	0008798	molecular_function	beta-aspartyl-peptidase activity
B	0016787	molecular_function	hydrolase activity
B	0042597	cellular_component	periplasmic space

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SD4 A 301

Chain	Residue
A	HIS150
A	HOH436
A	HOH437
A	ASP151
A	THR152
A	ASP172
A	ARG180
A	ASP183
A	THR203
A	GLY204
A	GLY206

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:10490104, ECO:0000269|PubMed:17157318, ECO:0000269|PubMed:20800597, ECO:0000269|PubMed:9685368

Chain	Residue	Details
A	THR152
B	THR152

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
A	ARG180
A	THR203
B	ARG180
B	THR203

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